ArticleMethods in molecular biology (Clifton, N.J.)2022
Isolating Anti-amyloid Antibodies from Yeast-Displayed Libraries.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Facile generation of drug-like conformational antibodies specific for amyloid fibrils.Nature chemical biology · 2025Article
- Directed evolution of drug-like Aβ conformation-specific antibodies.Frontiers in immunology · 2025Article
- Optimization of therapeutic antibodies for reduced self-association and non-specific binding via interpretable machine learning.Nature biomedical engineering · 2024Article
- Quantitative flow cytometric selection of tau conformational nanobodies specific for pathological aggregates.Frontiers in immunology · 2023Article
- Development of a pan-tau multivalent nanobody that binds tau aggregation motifs and recognizes pathological tau aggregates.Biotechnology progressArticle
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Authors and funding
4 authors.
Funding
Abstract
Conformational antibodies specific for amyloid-forming peptides and proteins are important for a range of biomedical applications, including detecting, inhibiting, and potentially treating protein aggregation disorders ranging from Alzheimer's to Parkinson's diseases. Generation of anti-amyloid antibodies is greatly complicated by the complex, heterogeneous and insoluble nature of amyloid antigens. Here we describe systematic methods for isolating and affinity maturing anti-amyloid antibodies using yeast surface display. Magnetic-activated cell sorting is used to sort single-chain antibody libraries positively for binding to amyloid antigens and negatively against the corresponding disaggregated antigens to remove antibodies that bind in a conformation-independent manner. Isolated lead antibody clones with conformational specificity are affinity matured via targeted CDR mutagenesis and magnetic-activated cell sorting.
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